Thyroid hormone (TH) is a key signal for oligodendrocyte differentiation and myelin formation during development and also stimulates remyelination in adult models of multiple sclerosis (MS) (Calzà L et al. Brain Res Revs 48, 339-346 (2005); incorporated by reference herein.) However, TH is not an acceptable long-term therapy due to there being virtually no therapeutic window in which remyelination can be achieved while avoiding the cardiotoxicity and bone demineralization associated with chronic hyperthyroidism. Some thyroid hormone analogs can activate thyroid hormone-responsive genes while avoiding the associated downsides of TH by exploiting molecular and physiological features of thyroid hormone receptors (Malm J et al. Mini Rev Med Chem 7, 79-86 (2007); incorporated by reference herein). These receptors are expressed in two major forms with heterogenous tissue distributions and overlapping but distinct sets of target genes (Yen P M, Physiol Rev 81, 1097-1142 (2001); incorporated by reference herein). TRu is enriched in the heart, brain, and bone while TR3 is enriched in the liver (O'Shea P J et al. Nucl Recept Signal 4, e011 (2006); incorporated by reference herein). Developing selective thyromimetics has been challenging due to the high sequence homology of thyroid hormone receptor subtypes—only one amino acid residue on the internal surface of the ligand binding domain cavity varies between the al and β1 forms. GC-1 was one of the first potent analogs that demonstrated significant TRβ-selectivity in vitro (Chiellini G et al. Chem Biol 5, 299-306 (1998) and Yoshihara H A I et al. J Med Chem 46, 3152-3161 (2003); both of which are incorporated by reference herein) and in vivo (Trost S U et al. Endocrinology 141, 3057-3064 (2000); Grover G J et al. Endocrinology 145, 1656-1661 (2004); and Baxter J D et al. Trends Endocrinol Metab 15, 154-157 (2004); all of which are incorporated by reference herein).